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. 1984 Dec;46(3):867–869. doi: 10.1128/iai.46.3.867-869.1984

Molecular characterization of glycoprotein antigens on surface of Treponema pallidum: comparison with nonpathogenic Treponema phagedenis biotype Reiter.

M Moskophidis, F Müller
PMCID: PMC261630  PMID: 6389370

Abstract

Four glycoproteins of Treponema pallidum were identified by intrinsic [14C]glucosamine labeling. Only two glycoproteins were demonstrated in T. phagedenis biotype Reiter with the same technique. Glycoproteins of both treponemes were characterized as antigens and shown to be localized within the outer membranes of the microorganisms.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Alderete J. F., Baseman J. B. Surface characterization of virulent Treponema pallidum. Infect Immun. 1980 Dec;30(3):814–823. doi: 10.1128/iai.30.3.814-823.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Alderete J. F., Baseman J. B. Surface-associated host proteins on virulent Treponema pallidum. Infect Immun. 1979 Dec;26(3):1048–1056. doi: 10.1128/iai.26.3.1048-1056.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Baseman J. B., Hayes E. C. Molecular characterization of receptor binding proteins and immunogens of virulent Treponema pallidum. J Exp Med. 1980 Mar 1;151(3):573–586. doi: 10.1084/jem.151.3.573. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fitzgerald T. J., Miller J. N., Sykes J. A. Treponema pallidum (Nichols strain) in tissue cultures: cellular attachment, entry, and survival. Infect Immun. 1975 May;11(5):1133–1140. doi: 10.1128/iai.11.5.1133-1140.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hanff P. A., Bishop N. H., Miller J. N., Lovett M. A. Humoral immune response in experimental syphilis to polypeptides of Treponema pallidum. J Immunol. 1983 Oct;131(4):1973–1977. [PubMed] [Google Scholar]
  6. Hanff P. A., Fehniger T. E., Miller J. N., Lovett M. A. Humoral immune response in human syphilis to polypeptides of Treponema pallidum. J Immunol. 1982 Sep;129(3):1287–1291. [PubMed] [Google Scholar]
  7. Lukehart S. A., Baker-Zander S. A., Gubish E. R., Jr Identification of Treponema pallidum antigens: comparison with a nonpathogenic treponeme. J Immunol. 1982 Aug;129(2):833–838. [PubMed] [Google Scholar]
  8. Marchalonis J. J. An enzymic method for the trace iodination of immunoglobulins and other proteins. Biochem J. 1969 Jun;113(2):299–305. doi: 10.1042/bj1130299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Moskophidis M., Müller F. Molecular analysis of immunoglobulins M and G immune response to protein antigens of Treponema pallidum in human syphilis. Infect Immun. 1984 Jan;43(1):127–132. doi: 10.1128/iai.43.1.127-132.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Nichols J. C., Baseman J. B. Carbon sources utilized by virulent Treponema pallidum. Infect Immun. 1975 Nov;12(5):1044–1050. doi: 10.1128/iai.12.5.1044-1050.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Thornburg R. W., Baseman J. B. Comparison of major protein antigens and protein profiles of Treponema pallidum and Treponema pertenue. Infect Immun. 1983 Nov;42(2):623–627. doi: 10.1128/iai.42.2.623-627.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

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